ID Q667H2_YERPS Unreviewed; 275 AA.
AC Q667H2;
DT 11-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 11-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE RecName: Full=THIF-type NAD/FAD binding fold domain-containing protein {ECO:0000259|Pfam:PF00899};
GN OrderedLocusNames=YPTB3020 {ECO:0000313|EMBL:CAH22258.1};
OS Yersinia pseudotuberculosis serotype I (strain IP32953).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=273123 {ECO:0000313|EMBL:CAH22258.1, ECO:0000313|Proteomes:UP000001011};
RN [1] {ECO:0000313|EMBL:CAH22258.1, ECO:0000313|Proteomes:UP000001011}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP32953 {ECO:0000313|Proteomes:UP000001011};
RX PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA Derbise A., Hauser L.J., Garcia E.;
RT "Insights into the evolution of Yersinia pestis through whole-genome
RT comparison with Yersinia pseudotuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
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DR EMBL; BX936398; CAH22258.1; -; Genomic_DNA.
DR RefSeq; WP_002212114.1; NZ_CP009712.1.
DR AlphaFoldDB; Q667H2; -.
DR SMR; Q667H2; -.
DR GeneID; 66844550; -.
DR KEGG; ypo:BZ17_3600; -.
DR KEGG; yps:YPTB3020; -.
DR PATRIC; fig|273123.14.peg.3780; -.
DR Proteomes; UP000001011; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR CDD; cd00755; YgdL_like; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR PANTHER; PTHR43267; TRNA THREONYLCARBAMOYLADENOSINE DEHYDRATASE; 1.
DR PANTHER; PTHR43267:SF1; TRNA THREONYLCARBAMOYLADENOSINE DEHYDRATASE; 1.
DR Pfam; PF00899; ThiF; 1.
DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 238..257
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 19..263
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
SQ SEQUENCE 275 AA; 29347 MW; 0413E3A74FD559ED CRC64;
MSTAYSEAYQ QRFGGIARLY GQQALALFSQ AHVCVIGIGG VGSWAAEALA RTGIGAITLI
DMDDVCVTNT NRQIHALRHN IGQAKTEVMA ERILAINPEC HVTCIDDFIT ADNVAELLNK
NFSYVIDAID SVRPKAALLS YCRRYKIPVV TTGGAGGQID PTRIAVVDLA KTIQDPLAAK
LRERLKSDFN VVKNSKGKLG IDCVFSSEPL VYPQADGSVC ASRSTAEGPK KMDCTSGFGS
ATMVTATFGF VAVSHVLKKM MAKAARQHES AATAS
//
